Enzymes
| UniProtKB help_outline | 1,248 proteins |
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- Name help_outline 5-(9Z-hexadecenoyloxy)-octadecanoate Identifier CHEBI:136369 Charge -1 Formula C34H63O4 InChIKeyhelp_outline HADGPAWFBKHJNM-SQFISAMPSA-M SMILEShelp_outline C(CCCC(CCCC(=O)[O-])OC(CCCCCCC/C=C\CCCCCC)=O)CCCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-hydroxy-octadecanoate Identifier CHEBI:136370 Charge -1 Formula C18H35O3 InChIKeyhelp_outline YTITYUDOZJUZBE-UHFFFAOYSA-M SMILEShelp_outline C(CCCCCCCCCC)CCC(CCCC([O-])=O)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (9Z)-hexadecenoate Identifier CHEBI:32372 Charge -1 Formula C16H29O2 InChIKeyhelp_outline SECPZKHBENQXJG-FPLPWBNLSA-M SMILEShelp_outline CCCCCC\C=C/CCCCCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:52092 | RHEA:52093 | RHEA:52094 | RHEA:52095 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs.
Parsons W.H., Kolar M.J., Kamat S.S., Cognetta A.B. III, Hulce J.J., Saez E., Kahn B.B., Saghatelian A., Cravatt B.F.
Enzyme classes may contain outlier members that share mechanistic, but not sequence or structural, relatedness with more common representatives. The functional annotation of such exceptional proteins can be challenging. Here, we use activity-based profiling to discover that the poorly characterize ... >> More
Enzyme classes may contain outlier members that share mechanistic, but not sequence or structural, relatedness with more common representatives. The functional annotation of such exceptional proteins can be challenging. Here, we use activity-based profiling to discover that the poorly characterized multipass transmembrane proteins AIG1 and ADTRP are atypical hydrolytic enzymes that depend on conserved threonine and histidine residues for catalysis. Both AIG1 and ADTRP hydrolyze bioactive fatty acid esters of hydroxy fatty acids (FAHFAs) but not other major classes of lipids. We identify multiple cell-active, covalent inhibitors of AIG1 and show that these agents block FAHFA hydrolysis in mammalian cells. These results indicate that AIG1 and ADTRP are founding members of an evolutionarily conserved class of transmembrane threonine hydrolases involved in bioactive lipid metabolism. More generally, our findings demonstrate how chemical proteomics can excavate potential cases of convergent or parallel protein evolution that defy conventional sequence- and structure-based predictions. << Less
Nat. Chem. Biol. 12:367-372(2016) [PubMed] [EuropePMC]
This publication is cited by 12 other entries.
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Branched fatty acid esters of hydroxy fatty acids are preferred substrates of the MODY8 protein carboxyl ester lipase.
Kolar M.J., Kamat S.S., Parsons W.H., Homan E.A., Maher T., Peroni O.D., Syed I., Fjeld K., Molven A., Kahn B.B., Cravatt B.F., Saghatelian A.
A recently discovered class of endogenous mammalian lipids, branched fatty acid esters of hydroxy fatty acids (FAHFAs), possesses anti-diabetic and anti-inflammatory activities. Here, we identified and validated carboxyl ester lipase (CEL), a pancreatic enzyme hydrolyzing cholesteryl esters and ot ... >> More
A recently discovered class of endogenous mammalian lipids, branched fatty acid esters of hydroxy fatty acids (FAHFAs), possesses anti-diabetic and anti-inflammatory activities. Here, we identified and validated carboxyl ester lipase (CEL), a pancreatic enzyme hydrolyzing cholesteryl esters and other dietary lipids, as a FAHFA hydrolase. Variants of CEL have been linked to maturity-onset diabetes of the young, type 8 (MODY8), and to chronic pancreatitis. We tested the FAHFA hydrolysis activity of the CEL MODY8 variant and found a modest increase in activity as compared with that of the normal enzyme. Together, the data suggest that CEL might break down dietary FAHFAs. << Less
Biochemistry 55:4636-4641(2016) [PubMed] [EuropePMC]
This publication is cited by 13 other entries.